Alzheimer’s disease researchers are hunting for new clues by comparing how different proteins in the brain are damaged in the same way. The work might also lead to greater understanding of other neurological disorders.

Studies have shown that brain diseases like Alzheimer’s and Parkinson’s worsen as increasingly large amounts of proteins in the brain become misfolded and start clumping together.

In developing new treatments for these progressive brain diseases, the focus has long been on distinct proteins, including those named amyloid and tau for Alzheimer’s. Now, though, some scientists are studying the life cycle of proteins, regardless of type, and what may go awry to lead to misfolding and ultimately disease.

A therapy that addresses the aggregation, or grouping together, of proteins in general, or the damage to them, could treat several neurodegenerative diseases rather than just one. At the Alzheimer’s Association International Conference in Washington that began Sunday, scientists from the New York University School of Medicine, Treventis Corp. and NeuroPhage Pharmaceuticals, among others, are presenting early evidence for three different compounds targeting protein misfolding and aggregation.

“If we have something that could really get to what’s basic and common to all the proteins that change and produce neurodegenerative disease, then what we really have is a pan-therapy that can really act anywhere” on any neurodegenerative disease, says Fernando Goni, a research professor in the department of neurology at the New York University School of Medicine.

Proteins are long chains of amino acids that make up the structure of the body’s tissues and organs and help them function correctly. Proteins not only must be built of the correct amino-acid building blocks, but also must have a particular shape.

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When the chains become misfolded in some progressive brain diseases, the misshapen proteins no longer do what they’re supposed to do and often stick to each other. When a single protein, called a monomer, binds with multiple forms of itself into a clustering known as an oligomer, that group becomes toxic and more difficult for the body to clear using its typical strategies, scientists believe.

In Alzheimer’s disease, when amyloid and tau proteins become misfolded, they gradually clump together and form plaques and tangles, which increase in quantity as the disease worsens. In Parkinson’s, the protein called alpha-synuclein clumps in a similar fashion. Other proteins called prions clump in conditions like mad-cow disease.

Treatments are available for the symptoms of Alzheimer’s, but they don’t slow the progression of the disease. Of the many so-called disease-modifying drugs in development, some have focused on amyloid and others on tau. None have succeeded yet, prompting scientists to look for other approaches.

How a cell handles protein damage and maintains the proper protein levels for cell functioning and the demands of the environment is “quite interesting and important to pursue further,” says Bradley Wise, chief of the neurobiology of aging branch at the National Institute on Aging.

Another reason scientists are targeting the protein-making process: It has become clearer in recent years that often more than one type of misfolded protein plays a role in neurodegenerative diseases. In brains examined in autopsies, many of those exhibiting Alzheimer’s pathology also have the characteristic Parkinson’s clumps of alpha-synuclein deposits and vice versa, says Richard Fisher, chief scientific officer at NeuroPhage, a Cambridge, Mass., company.

Scientists at NeuroPhage have identified an edge present on the surface of misfolded amyloid and tau proteins that is different from what’s found on undamaged proteins. They have developed a molecule to bind to that misshapen edge.

When it does, the misfolded protein can no longer bind inappropriately with other proteins, according to the researchers’ biochemical and animal work. In theory, the body will detect the misfolded proteins and, because they haven’t formed into difficult-to-clear clumps, get rid of them the way cells typically dispose of waste.

So far, in a laboratory dish, the compound identified by the NeuroPhage team blocks the spread of protein clumping. Mice genetically bred to produce human versions of Alzheimer’s tau or amyloid pathology that received weekly injections of the compound for 10 to 14 weeks became better over that period at recognizing new objects. They also grew more effective at remembering their way through a maze, compared with mice that didn’t receive the compound.

The mice haven’t exhibited side effects, Dr. Fisher says. He presented these yet-unpublished findings Sunday at the Alzheimer’s conference. An earlier description of the biochemical properties of the molecule itself was published last year in the Journal of Molecular Biology.

Neurophage is seeking permission from the Food and Drug Administration to start testing the compound in healthy human volunteers in January and hopes to start an early-stage multiple dosing and safety trial next summer, Dr. Fisher says.

Treventis, a Philadelphia-based biotech company, dubs itself a “protein misfolding company.” Using computer simulation to examine the shape of misfolded proteins, they have identified a region common to misfolded proteins and used that region to screen, using a computer database, 11.8 million known small molecules to find 130 that bind to it, according to Donald Weaver, director of Toronto Western Research Institute and a founder of the company. From there, they identified three that they thought had potential to become a drug and focused on developing one.

Presenting results from their first animal studies for the first time Sunday, the Treventis team showed that after giving a dose orally once a day for a week, they could see a decrease in the amount of amyloid and tau oligomers in the brains of mice bred to produce tau pathology. They also saw decreases in the level of amyloid in brain fluid.

Treventis, which is funded in part by the British nonprofit Wellcome Trust, is planning to continue its work in animals and hopes to begin its first efficacy trials in humans in 2018, says Marcy Taylor, director of biological sciences at the company.

Dr. Goni’s team at NYU, which will be presenting its latest results at the Alzheimer’s conference on Wednesday, has taken a different approach. They’re targeting proteins that have already bunched into oligomers, which scientists think are toxic.

The team took a chain of 13 amino acids that mimics one aspect of the structure of the oligomer, but which, when bound together by a particular chemical compound, doesn’t form into toxic clumps.

By introducing this foreign chain, or peptide, to the body, the body’s immune system makes antibodies against it. But because the peptide closely resembles part of the oligomers, the antibodies also work against the oligomers and clear the clumps from the body.

Dr. Goni introduced the foreign chain in mice, which produced many antibodies to it. They sifted through these antibodies to identify ones that were most effective at recognizing pathology. The team whittled them down to five.

In a dish holding sections of a brain with Alzheimer’s, the antibodies recognized tau and amyloid misfolded proteins in animals. They also have recognized prions.

The work in animals is time-intensive. Mice are raised to the age of 17 months, then infused with an antibody for at least two months, observed for a month to record any changes in behavior, then killed. Then their brains are analyzed.

“We might not have the magic bullet, but we’re very confident we’re on the right track,” Dr. Goni says.